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Protein

Vascular endothelial growth factor A

Gene

VEGFA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth.2 Publications

GO - Molecular functioni

  • chemoattractant activity Source: UniProtKB
  • cytokine activity Source: BHF-UCL
  • extracellular matrix binding Source: BHF-UCL
  • fibronectin binding Source: BHF-UCL
  • growth factor activity Source: BHF-UCL
  • heparin binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • neuropilin binding Source: BHF-UCL
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: BHF-UCL
  • receptor agonist activity Source: BHF-UCL
  • vascular endothelial growth factor receptor 1 binding Source: BHF-UCL
  • vascular endothelial growth factor receptor 2 binding Source: BHF-UCL
  • vascular endothelial growth factor receptor binding Source: UniProtKB

GO - Biological processi

  • activation of protein kinase activity Source: BHF-UCL
  • angiogenesis Source: UniProtKB
  • artery morphogenesis Source: BHF-UCL
  • basophil chemotaxis Source: UniProtKB
  • blood coagulation Source: Reactome
  • branching morphogenesis of an epithelial tube Source: BHF-UCL
  • camera-type eye morphogenesis Source: BHF-UCL
  • cardiac muscle fiber development Source: BHF-UCL
  • cardiac vascular smooth muscle cell development Source: BHF-UCL
  • cell maturation Source: BHF-UCL
  • cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • cellular response to hypoxia Source: MGI
  • cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  • commissural neuron axon guidance Source: BHF-UCL
  • coronary artery morphogenesis Source: BHF-UCL
  • coronary vein morphogenesis Source: BHF-UCL
  • dopaminergic neuron differentiation Source: BHF-UCL
  • endothelial cell chemotaxis Source: BHF-UCL
  • epithelial cell differentiation Source: BHF-UCL
  • eye photoreceptor cell development Source: BHF-UCL
  • growth Source: BHF-UCL
  • heart morphogenesis Source: BHF-UCL
  • induction of positive chemotaxis Source: UniProtKB
  • in utero embryonic development Source: BHF-UCL
  • kidney development Source: BHF-UCL
  • lactation Source: BHF-UCL
  • lung development Source: BHF-UCL
  • lymph vessel morphogenesis Source: BHF-UCL
  • macrophage differentiation Source: DFLAT
  • mammary gland alveolus development Source: BHF-UCL
  • mesoderm development Source: BHF-UCL
  • monocyte differentiation Source: DFLAT
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • nervous system development Source: UniProtKB
  • outflow tract morphogenesis Source: BHF-UCL
  • ovarian follicle development Source: BHF-UCL
  • patterning of blood vessels Source: BHF-UCL
  • platelet activation Source: Reactome
  • platelet degranulation Source: Reactome
  • positive chemotaxis Source: BHF-UCL
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of axon extension involved in axon guidance Source: BHF-UCL
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of branching involved in ureteric bud morphogenesis Source: BHF-UCL
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of cellular component movement Source: BHF-UCL
  • positive regulation of CREB transcription factor activity Source: BHF-UCL
  • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of endothelial cell migration Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of histone deacetylase activity Source: BHF-UCL
  • positive regulation of leukocyte migration Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: BHF-UCL
  • positive regulation of mast cell chemotaxis Source: UniProtKB
  • positive regulation of mesenchymal cell proliferation Source: BHF-UCL
  • positive regulation of neuroblast proliferation Source: BHF-UCL
  • positive regulation of p38MAPK cascade Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine autophosphorylation Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of positive chemotaxis Source: BHF-UCL
  • positive regulation of protein autophosphorylation Source: BHF-UCL
  • positive regulation of protein complex assembly Source: UniProtKB
  • positive regulation of protein kinase C signaling Source: BHF-UCL
  • positive regulation of protein kinase D signaling Source: BHF-UCL
  • positive regulation of protein localization to early endosome Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of receptor internalization Source: BHF-UCL
  • positive regulation of retinal ganglion cell axon guidance Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of vascular permeability Source: UniProtKB
  • post-embryonic camera-type eye development Source: BHF-UCL
  • primitive erythrocyte differentiation Source: BHF-UCL
  • regulation of cell shape Source: BHF-UCL
  • regulation of cGMP metabolic process Source: MGI
  • regulation of retinal ganglion cell axon guidance Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  • response to hypoxia Source: UniProtKB
  • surfactant homeostasis Source: BHF-UCL
  • tube formation Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • vascular endothelial growth factor signaling pathway Source: BHF-UCL
  • vasculogenesis Source: UniProtKB
  • VEGF-activated neuropilin signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_12380. VEGF ligand-receptor interactions.
REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.
REACT_264273. VEGFR2 mediated cell proliferation.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_264548. EPHA-mediated growth cone collapse.
REACT_318. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor A
Short name:
VEGF-A
Alternative name(s):
Vascular permeability factor
Short name:
VPF
Gene namesi
Name:VEGFA
Synonyms:VEGF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:12680. VEGFA.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • membrane Source: InterPro
  • platelet alpha granule lumen Source: Reactome
  • proteinaceous extracellular matrix Source: UniProtKB
  • secretory granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Microvascular complications of diabetes 1 (MVCD1)

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionPathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.

See also OMIM:603933

Organism-specific databases

MIMi603933. phenotype.
PharmGKBiPA37302.

Chemistry

DrugBankiDB08885. Aflibercept.
DB00112. Bevacizumab.
DB01136. Carvedilol.
DB06779. Dalteparin.
DB01120. Gliclazide.
DB01017. Minocycline.
DB01270. Ranibizumab.
DB05294. Vandetanib.

Polymorphism and mutation databases

BioMutaiVEGFA.
DMDMi17380528.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26262 PublicationsAdd
BLAST
Chaini27 – 232206Vascular endothelial growth factor APRO_0000023386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 94
Disulfide bondi77 – 77Interchain
Disulfide bondi83 ↔ 128
Disulfide bondi86 – 86Interchain
Disulfide bondi87 ↔ 130
Glycosylationi101 – 1011N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15692.
PRIDEiP15692.

PTM databases

PhosphoSiteiP15692.

Expressioni

Tissue specificityi

Isoform VEGF189, isoform VEGF165 and isoform VEGF121 are widely expressed. Isoform VEGF206 and isoform VEGF145 are not widely expressed. A higher level expression seen in pituitary tumors as compared to the pituitary gland.1 Publication

Inductioni

By hypoxia. Regulated by growth factors, cytokines, gonadotropins, nitric oxide, hypoglycemia and oncogenic mutations.1 Publication

Gene expression databases

BgeeiP15692.
ExpressionAtlasiP15692. baseline and differential.
GenevisibleiP15692. HS.

Organism-specific databases

HPAiCAB005429.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Also found as heterodimer with PGF (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself10EBI-1026643,EBI-1026643
FLT1P179484EBI-1026643,EBI-1026718
KDRP359686EBI-1026691,EBI-1005487
NRP1O147864EBI-1026643,EBI-1187100
NRP1O14786-24EBI-1026691,EBI-6285281

Protein-protein interaction databases

BioGridi113265. 27 interactions.
DIPiDIP-5740N.
IntActiP15692. 16 interactions.
MINTiMINT-2834049.
STRINGi9606.ENSP00000361125.

Structurei

Secondary structure

1
232
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 508Combined sources
Beta strandi51 – 6010Combined sources
Helixi61 – 644Combined sources
Helixi66 – 683Combined sources
Beta strandi71 – 8414Combined sources
Beta strandi93 – 10917Combined sources
Turni111 – 1133Combined sources
Beta strandi116 – 13116Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi194 – 1974Combined sources
Turni199 – 2013Combined sources
Beta strandi204 – 2085Combined sources
Helixi210 – 2145Combined sources
Turni215 – 2173Combined sources
Beta strandi219 – 2213Combined sources
Turni222 – 2254Combined sources
Beta strandi226 – 2283Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJ1X-ray2.40V/W34-135[»]
1CZ8X-ray2.40V/W40-133[»]
1FLTX-ray1.70V/W38-135[»]
1KATNMR-V/W37-135[»]
1KMXNMR-A183-232[»]
1MJVX-ray2.10A/B40-134[»]
1MKGX-ray2.50A/B/C/D40-134[»]
1MKKX-ray1.32A/B40-134[»]
1QTYX-ray2.70R/S/V/W34-135[»]
1TZHX-ray2.60V/W34-135[»]
1TZIX-ray2.80V34-135[»]
1VGHNMR-A180-232[»]
1VPFX-ray2.50A/B/C/D34-135[»]
1VPPX-ray1.90V/W34-135[»]
2FJGX-ray2.80V/W34-135[»]
2FJHX-ray3.10V/W34-135[»]
2QR0X-ray3.50C/D/I/J/O/P/U/V39-135[»]
2VGHNMR-A182-232[»]
2VPFX-ray1.93A/B/C/D/E/F/G/H34-135[»]
3BDYX-ray2.60V34-135[»]
3P9WX-ray2.41A/C/E/G35-138[»]
3QTKX-ray1.85A/B/C/D/E/F34-135[»]
3S1BX-ray2.90V38-133[»]
3S1KX-ray2.55V/W34-135[»]
3V2AX-ray3.20A27-140[»]
4DEQX-ray2.65A/B183-232[»]
4GLNX-ray1.60E/F34-135[»]
4GLSX-ray1.60E/F34-135[»]
4KZNX-ray1.71A39-135[»]
4QAFX-ray1.80C/D34-135[»]
4WPBX-ray3.11A/B34-135[»]
ProteinModelPortaliP15692.
SMRiP15692. Positions 39-133, 183-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15692.

Family & Domainsi

Sequence similaritiesi

Belongs to the PDGF/VEGF growth factor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG73329.
GeneTreeiENSGT00730000110791.
HOVERGENiHBG000105.
InParanoidiP15692.
KOiK05448.
PhylomeDBiP15692.

Family and domain databases

Gene3Di2.10.160.10. 1 hit.
2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
IPR027928. VEGF_C.
[Graphical view]
PfamiPF00341. PDGF. 1 hit.
PF14554. VEGF_C. 1 hit.
[Graphical view]
SMARTiSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
SSF57593. SSF57593. 1 hit.
PROSITEiPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]

Sequences (17)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 17 isoformsi produced by alternative promoter usage, alternative splicing and alternative initiation. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform VEGF206 (identifier: P15692-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS
60 70 80 90 100
YCHPIETLVD IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES
110 120 130 140 150
NITMQIMRIK PHQGQHIGEM SFLQHNKCEC RPKKDRARQE KKSVRGKGKG
160 170 180 190 200
QKRKRKKSRY KSWSVYVGAR CCLMPWSLPG PHPCGPCSER RKHLFVQDPQ
210 220 230
TCKCSCKNTD SRCKARQLEL NERTCRCDKP RR
Length:232
Mass (Da):27,042
Last modified:November 16, 2001 - v2
Checksum:iFB49F364446F4D01
GO
Isoform VEGF189 (identifier: P15692-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     166-182: Missing.

Show »
Length:215
Mass (Da):25,173
Checksum:i7B9759AD5871FF33
GO
Isoform VEGF183 (identifier: P15692-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     160-182: Missing.

Show »
Length:209
Mass (Da):24,422
Checksum:iF01CCEACD945D6CA
GO
Isoform VEGF165 (identifier: P15692-4) [UniParc]FASTAAdd to basket

Also known as: VEGF

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.

Show »
Length:191
Mass (Da):22,314
Checksum:iCCE57097DD3779BD
GO
Isoform VEGF148 (identifier: P15692-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
     215-215: A → M
     216-232: Missing.

Show »
Length:174
Mass (Da):20,218
Checksum:iAE88400CA7757644
GO
Isoform VEGF145 (identifier: P15692-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     166-226: Missing.

Show »
Length:171
Mass (Da):20,064
Checksum:iD02ECA735FF6E9F8
GO
Isoform VEGF165B (identifier: P15692-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
     227-232: CDKPRR → SLTRKD

Show »
Length:191
Mass (Da):22,259
Checksum:iD25243E540AC79BD
GO
Isoform VEGF121 (identifier: P15692-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-226: Missing.

Note: No experimental confirmation available.
Show »
Length:147
Mass (Da):17,219
Checksum:iDDF4D6994249BED6
GO
Isoform VEGF111 (identifier: P15692-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-226: Missing.

Note: No experimental confirmation available.
Show »
Length:137
Mass (Da):15,981
Checksum:i196B2BB49381BE87
GO
Isoform L-VEGF165 (identifier: P15692-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-141: K → N
     142-182: Missing.

Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications
Show »
Length:371
Mass (Da):40,738
Checksum:i053E9CA56725C07B
GO
Isoform L-VEGF121 (identifier: P15692-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     142-226: Missing.

Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications
Show »
Length:327
Mass (Da):35,643
Checksum:i8D6F969601B2A9EF
GO
Isoform L-VEGF189 (identifier: P15692-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     166-182: Missing.

Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications
Show »
Length:395
Mass (Da):43,597
Checksum:i8ADF6524B1835A2D
GO
Isoform L-VEGF206 (identifier: P15692-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM

Note: Gene prediction based on EST data. Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon.
Show »
Length:412
Mass (Da):45,467
Checksum:iAC807D3F21528D35
GO
Isoform 15 (identifier: P15692-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-182: KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH → N
     227-232: CDKPRR → SLTRKD

Note: Starts at an alternative upstream CUG codon.
Show »
Length:371
Mass (Da):40,683
Checksum:i1B89AFD7FABEC07B
GO
Isoform 16 (identifier: P15692-16) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     160-182: Missing.

Note: Starts at an alternative upstream CUG codon.
Show »
Length:389
Mass (Da):42,846
Checksum:i950279CF7A273A0E
GO
Isoform 17 (identifier: P15692-17) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-182: KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH → N
     215-215: A → M
     216-232: Missing.

Note: Starts at an alternative upstream CUG codon.
Show »
Length:354
Mass (Da):38,642
Checksum:i0152409399BAB1EB
GO
Isoform 18 (identifier: P15692-18) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     132-226: Missing.

Note: Starts at an alternative upstream CUG codon.
Show »
Length:317
Mass (Da):34,406
Checksum:iFDF27C1251E3B613
GO

Sequence cautioni

The sequence AAC63102.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAC63143.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAC19512.2 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAC19516.2 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871C → S in AAC63143 (PubMed:9450968).Curated
Sequence conflicti210 – 2101D → H in AAC63143 (PubMed:9450968).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MTDRQTDTAPSPSYHLLPGR RRTVDAAASRGQGPEPAPGG GVEGVGARGVALKLFVQLLG CSRFGGAVVRAGEAEPSGAA RSASSGREEPQPEEGEEEEE KEEERGPQWRLGARKPGSWT GEAAVCADSAPAARAPQALA RASGRGGRVARRGAEESGPP HSPSRRGSASRAGPGRASET M in isoform L-VEGF165, isoform L-VEGF121, isoform L-VEGF189, isoform L-VEGF206, isoform 15, isoform 16, isoform 17 and isoform 18. 1 PublicationVSP_038745
Alternative sequencei132 – 22695Missing in isoform VEGF111 and isoform 18. 1 PublicationVSP_026781Add
BLAST
Alternative sequencei141 – 18242KKSVR…LPGPH → N in isoform 15 and isoform 17. CuratedVSP_054111Add
BLAST
Alternative sequencei141 – 1411K → N in isoform VEGF148, isoform VEGF165, isoform VEGF165B and isoform L-VEGF165. 10 PublicationsVSP_004618
Alternative sequencei142 – 22685Missing in isoform VEGF121 and isoform L-VEGF121. 1 PublicationVSP_004620Add
BLAST
Alternative sequencei142 – 18241Missing in isoform VEGF148, isoform VEGF165, isoform VEGF165B and isoform L-VEGF165. 10 PublicationsVSP_004619Add
BLAST
Alternative sequencei160 – 18223Missing in isoform VEGF183 and isoform 16. 2 PublicationsVSP_004621Add
BLAST
Alternative sequencei166 – 22661Missing in isoform VEGF145. 1 PublicationVSP_004623Add
BLAST
Alternative sequencei166 – 18217Missing in isoform VEGF189 and isoform L-VEGF189. 2 PublicationsVSP_004622Add
BLAST
Alternative sequencei215 – 2151A → M in isoform VEGF148 and isoform 17. 1 PublicationVSP_004624
Alternative sequencei216 – 23217Missing in isoform VEGF148 and isoform 17. 1 PublicationVSP_004625Add
BLAST
Alternative sequencei227 – 2326CDKPRR → SLTRKD in isoform VEGF165B and isoform 15. 1 PublicationVSP_014783

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32977 mRNA. Translation: AAA35789.1.
M27281 mRNA. Translation: AAA36807.1.
M63978
, M63971, M63972, M63973, M63974, M63975, M63976, M63977 Genomic DNA. Translation: AAA36804.1.
S85192 mRNA. Translation: AAC63102.1. Different initiation.
AH006909 Genomic DNA. Translation: AAC63101.1.
X62568 mRNA. Translation: CAA44447.1.
AJ010438 mRNA. Translation: CAA09179.1.
AF022375 mRNA. Translation: AAC63143.1. Sequence problems.
AF091352 mRNA. Translation: AAD55345.1.
AF430806 mRNA. Translation: AAL27435.1.
AB021221 mRNA. Translation: BAA78418.1.
AF214570 mRNA. Translation: AAF19659.1.
AY047581 mRNA. Translation: AAK95847.1.
AF486837 mRNA. Translation: AAM03108.1.
AY766116 mRNA. Translation: AAV34601.1.
DQ229900 mRNA. Translation: ABB58912.1.
AB451322 mRNA. Translation: BAG70136.1.
AB451451 mRNA. Translation: BAG70265.1.
AL136131 Genomic DNA. Translation: CAC19512.2. Sequence problems.
AL136131 Genomic DNA. Translation: CAC19513.2.
AL136131 Genomic DNA. Translation: CAC19515.2.
AL136131 Genomic DNA. Translation: CAC19516.2. Sequence problems.
CH471081 Genomic DNA. Translation: EAX04229.1.
BC065522 mRNA. Translation: AAH65522.2.
AF437895 Genomic DNA. Translation: AAL27630.1.
AF062645 mRNA. Translation: AAC16730.1.
CCDSiCCDS34457.1. [P15692-14]
CCDS34458.1. [P15692-11]
CCDS47432.1. [P15692-15]
CCDS47433.1. [P15692-16]
CCDS47434.1. [P15692-12]
CCDS47435.1. [P15692-17]
CCDS4907.2. [P15692-13]
CCDS55007.1. [P15692-18]
CCDS55008.1. [P15692-3]
CCDS55009.1. [P15692-2]
CCDS55010.1. [P15692-1]
CCDS55011.1. [P15692-5]
CCDS55012.1. [P15692-4]
CCDS55013.1. [P15692-8]
CCDS55014.1. [P15692-9]
CCDS55015.1. [P15692-10]
PIRiA41551.
RefSeqiNP_001020537.2. NM_001025366.2. [P15692-14]
NP_001020538.2. NM_001025367.2. [P15692-16]
NP_001020539.2. NM_001025368.2. [P15692-11]
NP_001020540.2. NM_001025369.2. [P15692-17]
NP_001020541.2. NM_001025370.2. [P15692-12]
NP_001028928.1. NM_001033756.2. [P15692-15]
NP_001165093.1. NM_001171622.1. [P15692-18]
NP_001165094.1. NM_001171623.1. [P15692-1]
NP_001165095.1. NM_001171624.1. [P15692-2]
NP_001165096.1. NM_001171625.1. [P15692-3]
NP_001165097.1. NM_001171626.1. [P15692-4]
NP_001165098.1. NM_001171627.1. [P15692-5]
NP_001165099.1. NM_001171628.1. [P15692-9]
NP_001165100.1. NM_001171629.1. [P15692-8]
NP_001165101.1. NM_001171630.1. [P15692-10]
NP_001191313.1. NM_001204384.1. [P15692-6]
NP_001191314.1. NM_001204385.1.
NP_001273973.1. NM_001287044.1.
NP_003367.4. NM_003376.5. [P15692-13]
UniGeneiHs.73793.

Genome annotation databases

EnsembliENST00000372077; ENSP00000361148; ENSG00000112715. [P15692-9]
ENST00000457104; ENSP00000409911; ENSG00000112715. [P15692-10]
ENST00000518689; ENSP00000430829; ENSG00000112715. [P15692-3]
ENST00000518824; ENSP00000430002; ENSG00000112715. [P15692-8]
ENST00000523125; ENSP00000429008; ENSG00000112715. [P15692-5]
ENST00000523873; ENSP00000430479; ENSG00000112715.
ENST00000523950; ENSP00000429643; ENSG00000112715. [P15692-4]
GeneIDi7422.
KEGGihsa:7422.
UCSCiuc003owd.3. human. [P15692-5]
uc003owe.3. human. [P15692-4]
uc003owf.3. human. [P15692-13]
uc003owg.3. human. [P15692-3]
uc003owh.3. human. [P15692-1]
uc003owi.3. human. [P15692-8]
uc003owj.3. human. [P15692-9]
uc010jyx.3. human. [P15692-10]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage, Alternative splicing

Cross-referencesi

Web resourcesi

R&D Systems' cytokine mini-reviews: VEGF
Wikipedia

VEGF entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32977 mRNA. Translation: AAA35789.1.
M27281 mRNA. Translation: AAA36807.1.
M63978
, M63971, M63972, M63973, M63974, M63975, M63976, M63977 Genomic DNA. Translation: AAA36804.1.
S85192 mRNA. Translation: AAC63102.1. Different initiation.
AH006909 Genomic DNA. Translation: AAC63101.1.
X62568 mRNA. Translation: CAA44447.1.
AJ010438 mRNA. Translation: CAA09179.1.
AF022375 mRNA. Translation: AAC63143.1. Sequence problems.
AF091352 mRNA. Translation: AAD55345.1.
AF430806 mRNA. Translation: AAL27435.1.
AB021221 mRNA. Translation: BAA78418.1.
AF214570 mRNA. Translation: AAF19659.1.
AY047581 mRNA. Translation: AAK95847.1.
AF486837 mRNA. Translation: AAM03108.1.
AY766116 mRNA. Translation: AAV34601.1.
DQ229900 mRNA. Translation: ABB58912.1.
AB451322 mRNA. Translation: BAG70136.1.
AB451451 mRNA. Translation: BAG70265.1.
AL136131 Genomic DNA. Translation: CAC19512.2. Sequence problems.
AL136131 Genomic DNA. Translation: CAC19513.2.
AL136131 Genomic DNA. Translation: CAC19515.2.
AL136131 Genomic DNA. Translation: CAC19516.2. Sequence problems.
CH471081 Genomic DNA. Translation: EAX04229.1.
BC065522 mRNA. Translation: AAH65522.2.
AF437895 Genomic DNA. Translation: AAL27630.1.
AF062645 mRNA. Translation: AAC16730.1.
CCDSiCCDS34457.1. [P15692-14]
CCDS34458.1. [P15692-11]
CCDS47432.1. [P15692-15]
CCDS47433.1. [P15692-16]
CCDS47434.1. [P15692-12]
CCDS47435.1. [P15692-17]
CCDS4907.2. [P15692-13]
CCDS55007.1. [P15692-18]
CCDS55008.1. [P15692-3]
CCDS55009.1. [P15692-2]
CCDS55010.1. [P15692-1]
CCDS55011.1. [P15692-5]
CCDS55012.1. [P15692-4]
CCDS55013.1. [P15692-8]
CCDS55014.1. [P15692-9]
CCDS55015.1. [P15692-10]
PIRiA41551.
RefSeqiNP_001020537.2. NM_001025366.2. [P15692-14]
NP_001020538.2. NM_001025367.2. [P15692-16]
NP_001020539.2. NM_001025368.2. [P15692-11]
NP_001020540.2. NM_001025369.2. [P15692-17]
NP_001020541.2. NM_001025370.2. [P15692-12]
NP_001028928.1. NM_001033756.2. [P15692-15]
NP_001165093.1. NM_001171622.1. [P15692-18]
NP_001165094.1. NM_001171623.1. [P15692-1]
NP_001165095.1. NM_001171624.1. [P15692-2]
NP_001165096.1. NM_001171625.1. [P15692-3]
NP_001165097.1. NM_001171626.1. [P15692-4]
NP_001165098.1. NM_001171627.1. [P15692-5]
NP_001165099.1. NM_001171628.1. [P15692-9]
NP_001165100.1. NM_001171629.1. [P15692-8]
NP_001165101.1. NM_001171630.1. [P15692-10]
NP_001191313.1. NM_001204384.1. [P15692-6]
NP_001191314.1. NM_001204385.1.
NP_001273973.1. NM_001287044.1.
NP_003367.4. NM_003376.5. [P15692-13]
UniGeneiHs.73793.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJ1X-ray2.40V/W34-135[»]
1CZ8X-ray2.40V/W40-133[»]
1FLTX-ray1.70V/W38-135[»]
1KATNMR-V/W37-135[»]
1KMXNMR-A183-232[»]
1MJVX-ray2.10A/B40-134[»]
1MKGX-ray2.50A/B/C/D40-134[»]
1MKKX-ray1.32A/B40-134[»]
1QTYX-ray2.70R/S/V/W34-135[»]
1TZHX-ray2.60V/W34-135[»]
1TZIX-ray2.80V34-135[»]
1VGHNMR-A180-232[»]
1VPFX-ray2.50A/B/C/D34-135[»]
1VPPX-ray1.90V/W34-135[»]
2FJGX-ray2.80V/W34-135[»]
2FJHX-ray3.10V/W34-135[»]
2QR0X-ray3.50C/D/I/J/O/P/U/V39-135[»]
2VGHNMR-A182-232[»]
2VPFX-ray1.93A/B/C/D/E/F/G/H34-135[»]
3BDYX-ray2.60V34-135[»]
3P9WX-ray2.41A/C/E/G35-138[»]
3QTKX-ray1.85A/B/C/D/E/F34-135[»]
3S1BX-ray2.90V38-133[»]
3S1KX-ray2.55V/W34-135[»]
3V2AX-ray3.20A27-140[»]
4DEQX-ray2.65A/B183-232[»]
4GLNX-ray1.60E/F34-135[»]
4GLSX-ray1.60E/F34-135[»]
4KZNX-ray1.71A39-135[»]
4QAFX-ray1.80C/D34-135[»]
4WPBX-ray3.11A/B34-135[»]
ProteinModelPortaliP15692.
SMRiP15692. Positions 39-133, 183-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113265. 27 interactions.
DIPiDIP-5740N.
IntActiP15692. 16 interactions.
MINTiMINT-2834049.
STRINGi9606.ENSP00000361125.

Chemistry

BindingDBiP15692.
ChEMBLiCHEMBL1783.
DrugBankiDB08885. Aflibercept.
DB00112. Bevacizumab.
DB01136. Carvedilol.
DB06779. Dalteparin.
DB01120. Gliclazide.
DB01017. Minocycline.
DB01270. Ranibizumab.
DB05294. Vandetanib.
GuidetoPHARMACOLOGYi2644.

PTM databases

PhosphoSiteiP15692.

Polymorphism and mutation databases

BioMutaiVEGFA.
DMDMi17380528.

Proteomic databases

PaxDbiP15692.
PRIDEiP15692.

Protocols and materials databases

DNASUi7422.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372077; ENSP00000361148; ENSG00000112715. [P15692-9]
ENST00000457104; ENSP00000409911; ENSG00000112715. [P15692-10]
ENST00000518689; ENSP00000430829; ENSG00000112715. [P15692-3]
ENST00000518824; ENSP00000430002; ENSG00000112715. [P15692-8]
ENST00000523125; ENSP00000429008; ENSG00000112715. [P15692-5]
ENST00000523873; ENSP00000430479; ENSG00000112715.
ENST00000523950; ENSP00000429643; ENSG00000112715. [P15692-4]
GeneIDi7422.
KEGGihsa:7422.
UCSCiuc003owd.3. human. [P15692-5]
uc003owe.3. human. [P15692-4]
uc003owf.3. human. [P15692-13]
uc003owg.3. human. [P15692-3]
uc003owh.3. human. [P15692-1]
uc003owi.3. human. [P15692-8]
uc003owj.3. human. [P15692-9]
uc010jyx.3. human. [P15692-10]

Organism-specific databases

CTDi7422.
GeneCardsiGC06P043737.
HGNCiHGNC:12680. VEGFA.
HPAiCAB005429.
MIMi192240. gene.
603933. phenotype.
neXtProtiNX_P15692.
PharmGKBiPA37302.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG73329.
GeneTreeiENSGT00730000110791.
HOVERGENiHBG000105.
InParanoidiP15692.
KOiK05448.
PhylomeDBiP15692.

Enzyme and pathway databases

ReactomeiREACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_12380. VEGF ligand-receptor interactions.
REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.
REACT_264273. VEGFR2 mediated cell proliferation.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_264548. EPHA-mediated growth cone collapse.
REACT_318. Platelet degranulation.

Miscellaneous databases

ChiTaRSiVEGFA. human.
EvolutionaryTraceiP15692.
GeneWikiiVascular_endothelial_growth_factor_A.
GenomeRNAii7422.
NextBioi29060.
PROiP15692.
SOURCEiSearch...

Gene expression databases

BgeeiP15692.
ExpressionAtlasiP15692. baseline and differential.
GenevisibleiP15692. HS.

Family and domain databases

Gene3Di2.10.160.10. 1 hit.
2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
IPR027928. VEGF_C.
[Graphical view]
PfamiPF00341. PDGF. 1 hit.
PF14554. VEGF_C. 1 hit.
[Graphical view]
SMARTiSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
SSF57593. SSF57593. 1 hit.
PROSITEiPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Vascular endothelial growth factor is a secreted angiogenic mitogen."
    Leung D.W., Cachianes G., Kuang W.-J., Goeddel D.V., Ferrara N.
    Science 246:1306-1309(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF189 AND VEGF165).
  2. "Vascular permeability factor, an endothelial cell mitogen related to PDGF."
    Keck P.J., Hauser S.D., Krivi G., Sanzo K., Warren T., Feder J., Connolly D.T.
    Science 246:1309-1312(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF189), PARTIAL PROTEIN SEQUENCE.
  3. "The human gene for vascular endothelial growth factor. Multiple protein forms are encoded through alternative exon splicing."
    Tischer E., Mitchell R., Hartman T., Silva M., Gospodarowicz D., Fiddes J.C., Abraham J.A.
    J. Biol. Chem. 266:11947-11954(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM VEGF189).
  4. "The vascular endothelial growth factor family: identification of a fourth molecular species and characterization of alternative splicing of RNA."
    Houck K.A., Ferrara N., Winer J., Cachianes G., Li B., Leung D.W.
    Mol. Endocrinol. 5:1806-1814(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM VEGF206).
  5. "AIDS-associated Kaposi's sarcoma cells in culture express vascular endothelial growth factor."
    Weindel K., Marme D., Weich H.A.
    Biochem. Biophys. Res. Commun. 183:1167-1174(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
  6. "VEGF145, a secreted vascular endothelial growth factor isoform that binds to extracellular matrix."
    Poltorak Z., Cohen T., Sivan R., Kandelis Y., Spira G., Vlodavsky I., Keshet E., Neufeld G.
    J. Biol. Chem. 272:7151-7158(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF145).
  7. "Identification and characterization of a new splicing variant of vascular endothelial growth factor: VEGF183."
    Lei J., Jiang A., Pei D.
    Biochim. Biophys. Acta 1443:400-406(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF183).
    Tissue: Kidney.
  8. "Identification of a human VPF/VEGF 3' untranslated region mediating hypoxia-induced mRNA stability."
    Claffey K.P., Shih S.-C., Mullen A., Dziennis S., Cusick J.L., Abrams K.R., Lee S.W., Detmar M.
    Mol. Biol. Cell 9:469-481(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-VEGF165).
    Tissue: Mammary gland.
  9. "Heterogeneous vascular endothelial growth factor (VEGF) isoform mRNA and receptor mRNA expression in human glomeruli, and the identification of VEGF148 mRNA, a novel truncated splice variant."
    Whittle C.J., Gillespie K.M., Harrison R., Mathieson P.W., Harper S.J.
    Clin. Sci. 97:303-312(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF148).
    Tissue: Renal glomerulus.
  10. "VEGF165b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma."
    Bates D.O., Cui T.-G., Doughty J.M., Winkler M., Sugiono M., Shields J.D., Peat D., Gillatt D., Harper S.J.
    Cancer Res. 62:4123-4131(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165B).
    Tissue: Kidney.
  11. "Human cDNA for the vascular endothelial growth factor isoform VEGF165."
    Murata H., Fukushima J., Hattori S., Okuda K., Yanagi H.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
    Tissue: Hemangioendothelioma.
  12. "Human cDNA for vascular endothelial growth factor isoform VEGF121."
    Sato J.D., Whitney R.G.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF121).
  13. "Cloning of vascular endothelial growth factor (VEGF) cDNA."
    Liu J., Peng X., Yuan J., Qiang B.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
  14. "Cloning and identification of vascular endothelial growth factor isoform VEGF165."
    Shan Z.X., Yu X.Y., Lin Q.X., Fu Y.H., Zheng M., Tan H.H., Lin S.G.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
    Tissue: Heart.
  15. "Cloning and characterization of VEGF from LNCaP cells, a line of prostate cancer cells."
    Koul S., Johnson T., Meacham R.B., Koul H.K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
  16. "VEGF111, a new VEGF-A variant lacking exons 5, 6 and 7."
    Mineur P.J., Colige A.C., Lambert C.A.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF111).
  17. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF165).
  18. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  19. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  20. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L-VEGF121).
    Tissue: Lung.
  21. SeattleSNPs variation discovery resource
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-232.
  22. "Synthesis and assembly of functionally active human vascular endothelial growth factor homodimers in insect cells."
    Fiebich B.L., Jaeger B., Schoellmann C., Weindel K., Wilting J., Kochs G., Marme D., Hug H., Weich H.A.
    Eur. J. Biochem. 211:19-26(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41.
  23. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41.
  24. "Human vascular permeability factor. Isolation from U937 cells."
    Connolly D.T., Olander J.V., Heuvelman D., Nelson R., Monsell R., Siegel N., Haymore B.L., Leimgruber R., Feder J.
    J. Biol. Chem. 264:20017-20024(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 27-36; 43-50 AND 59-81.
  25. "Human Muller cells express VEGF183, a novel spliced variant of vascular endothelial growth factor."
    Jingjing L., Xue Y., Agarwal N., Roque R.S.
    Invest. Ophthalmol. Vis. Sci. 40:752-759(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-209 (ISOFORM VEGF183).
    Tissue: Retina.
  26. "A precursor form of vascular endothelial growth factor arises by initiation from an upstream in-frame CUG codon."
    Tee M.K., Jaffe R.B.
    Biochem. J. 359:219-226(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING, SUBCELLULAR LOCATION.
  27. "Vascular endothelial growth factor induces cyclooxygenase-dependent proliferation of endothelial cells via the VEGF-2 receptor."
    Murphy J.F., Fitzgerald D.J.
    FASEB J. 15:1667-1669(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "New vascular endothelial growth factor isoform generated by internal ribosome entry site-driven CUG translation initiation."
    Huez I., Bornes S., Bresson D., Creancier L., Prats H.
    Mol. Endocrinol. 15:2197-2210(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM L-VEGF189), PROCESSING, SUBCELLULAR LOCATION.
  29. "A common polymorphism in the 5'-untranslated region of the VEGF gene is associated with diabetic retinopathy in type 2 diabetes."
    Awata T., Inoue K., Kurihara S., Ohkubo T., Watanabe M., Inukai K., Inoue I., Katayama S.
    Diabetes 51:1635-1639(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MICROVASCULAR COMPLICATIONS OF DIABETES.
  30. "VEGF165b, an inhibitory vascular endothelial growth factor splice variant: mechanism of action, in vivo effect on angiogenesis and endogenous protein expression."
    Woolard J., Wang W.-Y., Bevan H.S., Qiu Y., Morbidelli L., Pritchard-Jones R.O., Cui T.-G., Sugiono M., Waine E., Perrin R., Foster R., Digby-Bell J., Shields J.D., Whittles C.E., Mushens R.E., Gillatt D.A., Ziche M., Harper S.J., Bates D.O.
    Cancer Res. 64:7822-7835(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM VEGF165B).
  31. "Control of the vascular endothelial growth factor internal ribosome entry site (IRES) activity and translation initiation by alternatively spliced coding sequences."
    Bornes S., Boulard M., Hieblot C., Zanibellato C., Iacovoni J.S., Prats H., Touriol C.
    J. Biol. Chem. 279:18717-18726(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121; L-VEGF165 AND L-VEGF189).
  32. "Nuclear localization of long-VEGF is associated with hypoxia and tumor angiogenesis."
    Rosenbaum-Dekel Y., Fuchs A., Yakirevich E., Azriel A., Mazareb S., Resnick M.B., Levi B.Z.
    Biochem. Biophys. Res. Commun. 332:271-278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING, SUBCELLULAR LOCATION.
  33. "Minimal active domain and mechanism of action of the angiogenesis inhibitor histidine-rich glycoprotein."
    Dixelius J., Olsson A.K., Thulin A., Lee C., Johansson I., Claesson-Welsh L.
    Cancer Res. 66:2089-2097(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION.
  34. "RSUME is implicated in HIF-1-induced VEGF-A production in pituitary tumour cells."
    Shan B., Gerez J., Haedo M., Fuertes M., Theodoropoulou M., Buchfelder M., Losa M., Stalla G.K., Arzt E., Renner U.
    Endocr. Relat. Cancer 19:13-27(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  35. "Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site."
    Muller Y.A., Li B., Christinger H.W., Wells J.A., Cunningham B.C., de Vos A.M.
    Proc. Natl. Acad. Sci. U.S.A. 94:7192-7197(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-135.
  36. "1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor."
    Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A., Starovasnik M.A.
    Protein Sci. 6:2250-2260(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 34-135.
  37. "The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93-A resolution: multiple copy flexibility and receptor binding."
    Muller Y.A., Christinger H.W., Keyt B.A., de Vos A.M.
    Structure 5:1325-1338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 34-135.
  38. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 39-134.
  39. "Solution structure of the heparin-binding domain of vascular endothelial growth factor."
    Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A., Starovasnik M.A.
    Structure 6:637-648(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 137-215.

Entry informationi

Entry nameiVEGFA_HUMAN
AccessioniPrimary (citable) accession number: P15692
Secondary accession number(s): B5BU86
, H0Y2S8, H0Y407, H0Y414, H0Y462, H0Y8N2, H3BLW7, O60720, O75875, Q074Z4, Q16889, Q5UB46, Q6P0P5, Q96KJ0, Q96L82, Q96NW5, Q9H1W8, Q9H1W9, Q9UH58, Q9UL23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 16, 2001
Last modified: July 22, 2015
This is version 202 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.